A Very Stableβ-Glucosidase from aCandida molischianaMutant Strain: Enzymatic Properties, Sequencing, and Homology with Other Yeastβ-Glucosidases

Janbon, Guilhem; Derancourt, Jean; Chemardin, Patrick; Arnaud, A.; Galzy, P.

doi:10.1271/bbb.59.1320

Cited by 16 publications

(5 citation statements)

References 5 publications

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“…Among these microbes, Trichoderma reesei is the most commonly used strain and is the first choice for cellulase production (Saha and Bothast 1996). It has a high capacity for producing cellulases and degrades cellulose in the presence of insoluble cellulose, semicellulose and some plant biomasses (Janbon et al 1995;Coughlan 1985). Reese (1977) proposed the C1-Cx hypothesis to illustrate the mechanism of cellulose enzymatic hydrolysis.…”

Section: Introductionmentioning

confidence: 99%

Synergistic effect of thermostable β-glucosidase TN0602 and cellulase on cellulose hydrolysis

et al. 2017

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Thermophilic enzymes have many potential benefits in industrial production with increased flexibility related to process configurations. A thermostable β-glucosidase from Thermotoga naphthophila RUK-10 was found to possess catalytic activity for cellobiose hydrolysis with a high potential for application in biomass conversion. The aggregation of cellobiose often has an inhibitory effect on cellobiohydrolases and endoglucanases during cellulose hydrolysis. The presence of β-glucosidases has a significant effect on reducing inhibition from hydrolytic products by hydrolysing the intermedia cellobiose. In this study, β-glucosidase TN0602 exhibited a high tolerance to glucose and high thermostability even after a long incubation (>72 h). Additionally, supplementing β-glucosidase TN0602 with microcrystalline cellulose, untreated corn straw and steam-exploded corn straw hydrolysis reactions containing a commercial cellulase led to an increased conversion rate in released glucose compared to hydrolysis without the addition of β-glucosidase (15.82, 30.62 and 35.21%, respectively); the increase of conversion rates were 61.86, 93.50 and 94.55%. It was thus shown that an obvious synergistic effect exists between TN0602 and cellulases for cellulose hydrolysis, suggesting its potential as a component of enzymatic cocktails for the conversion of lignocellulosic biomass to other chemicals.

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Section: Introductionmentioning

confidence: 99%

Synergistic effect of thermostable β-glucosidase TN0602 and cellulase on cellulose hydrolysis

et al. 2017

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“…The β-glucosidase could function at low pH value (optimum pH 3.5); it is also very stable (78% activity recovered after 145 h at pH 3.5 and 30 °C) and had enhanced activity in the presence of ethanol (Janbon et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

A Very Efficient β-Glucosidase Catalyst for the Hydrolysis of Flavor Precursors of Wines and Fruit Juices

Gueguen¹,

Chemardin²,

Janbon³

et al. 1996

J. Agric. Food Chem.

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121

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Candida molischiana 35M5N β-glucosidase was immobilized to Duolite A-568 resin. Higher immobilization efficiency (86%) was achieved with citrate−phosphate buffer (0.1 M) at pH 4. The study of the immobilized β-glucosidase demonstrated that the physicochemical properties were similar to those of the free enzyme. Free and immobilized β-glucosidase were used to treat muscat wine and apricot fruit juice. GC−MS analysis indicated a significant increase in the flavor compounds nerol, geraniol, linalool, 2-phenylethanol, and benzyl alcohol in the muscat wine and linalool, α- and γ-terpinene, α-terpineol, 2-phenylethanol, and α-pinene in the apricot fruit juice. The immobilized β-glucosidase was found to be very stable under fruit juice or wine conditions and could be used repeatedly for several hydrolyses of bound aroma. The efficiency of this experimental catalyst was successfully tested with several fruit juices and wines containing various amounts of precursors. Keywords: Wines; fruit juices; aroma precursors; β-glucosidase; immobilization

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“…Extracellular β-glucosidases from C. molischiana strains CBS136, 35, and 35M5N have been purified and characterized. The former showed quite different properties with respect to the other two β-glucosidases, possibly indicating the capability of C. molischiana to produce different β-glucosidases (Gonde ´et al, 1985;Janbon et al, 1995a;Vasserot et al, 1991). BGLN protein purified from strain YCB3 5 showed different properties, such as molecular mass and substrate specificity against arbutin and salicin, when compared with the protein purified from C. molischiana CBS136 (Gonde ´et al, 1985).…”

Section: Discussionmentioning

confidence: 98%

“…These differences could reflect the existence of at least two different β-glucosidase-encoding genes. However, the kinetic characteristics of the C. molischiana 35 protein (Vasserot et al, 1991), the amino acid sequence of which was the basis for the cloning of the bgln gene (Janbon et al, 1995a), showed also striking differences with BGLN from YCB3 5 , when in theory both proteins are encoded by the same bgln gene. To detect possible polymerization mistakes introduced by the Taq polymerase during the PCR reactions, ≈1700 nucleotides (nt) bgln gene were sequenced, including 1450 nt from the coding region (results not shown).…”

Section: Discussionmentioning

confidence: 99%

Heterologous Expression of aCandida molischianaAnthocyanin-β-glucosidase in a Wine Yeast Strain

Sánchez-Torres

González-Candelas

Ramón

1998

J. Agric. Food Chem.

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A recombinant wine yeast strain expressing the Candidamolischiana bgln gene encoding a beta-glucosidase/anthocyanase under the control of the Saccharomyces cerevisiae actin gene promoter has been constructed. The corresponding protein, BGLN, was mainly located on the cell wall. BGLN was purified in a single chromotagraphic step, and different physicochemical and kinetic properties have been determined. BGLN showed maximum activity against the artificial substrate p-nitrophenyl beta-D-glucopyranoside. It also hydrolyzed salicin, p-nitrophenyl beta-D-xyloside, cellobiose, and arbutin to a lesser extent. Fructose and SO(2) did not affect enzyme activity, which was activated by ethanol, while glucose was a strong competitive inhibitor. The purified BGLN showed a novel anthocyanase decolorizing capability on red wines. This anthocyanase activity was readily observed during microvinification experiments. However, the physicochemical characteristics of the wines obtained with the recombinant wine yeast strain were indistinguishable from those obtained with the parental strain.

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A Very Stableβ-Glucosidase from aCandida molischianaMutant Strain: Enzymatic Properties, Sequencing, and Homology with Other Yeastβ-Glucosidases

Cited by 16 publications

References 5 publications

Synergistic effect of thermostable β-glucosidase TN0602 and cellulase on cellulose hydrolysis

Synergistic effect of thermostable β-glucosidase TN0602 and cellulase on cellulose hydrolysis

A Very Efficient β-Glucosidase Catalyst for the Hydrolysis of Flavor Precursors of Wines and Fruit Juices

Heterologous Expression of aCandida molischianaAnthocyanin-β-glucosidase in a Wine Yeast Strain

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